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6XPC

Structure of human GGT1 in complex with full GSH molecule

Functional Information from GO Data
ChainGOidnamespacecontents
A0006751biological_processglutathione catabolic process
A0036374molecular_functionglutathione hydrolase activity
B0006751biological_processglutathione catabolic process
B0036374molecular_functionglutathione hydrolase activity
Functional Information from PROSITE/UniProt
site_idPS00462
Number of Residues25
DetailsG_GLU_TRANSPEPTIDASE Gamma-glutamyltranspeptidase signature. TAHlSVvaedGSaVSaTsTINlyFG
ChainResidueDetails
BTHR381-GLY405

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Nucleophile => ECO:0000269|PubMed:17924658, ECO:0000269|PubMed:26013825
ChainResidueDetails
BTHR381

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:24047895, ECO:0000269|PubMed:26013825
ChainResidueDetails
BSER451
BTHR399

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:26013825
ChainResidueDetails
BGLY474
BASP423

site_idSWS_FT_FI4
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:15084671, ECO:0000269|PubMed:17924658, ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:20622017, ECO:0000269|PubMed:24047895, ECO:0000269|PubMed:26013825
ChainResidueDetails
BASN511

site_idSWS_FT_FI5
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:17924658, ECO:0000269|PubMed:20622017, ECO:0000269|PubMed:24047895, ECO:0000269|PubMed:26013825
ChainResidueDetails
AASN266
AASN344

site_idSWS_FT_FI6
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:20622017
ChainResidueDetails
AASN297

219869

PDB entries from 2024-05-15

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